Golgi Apparatus and Melanogenesis: Ultrastructural Study of a Human Cellular Blue Nevus (Melanocytoma)

1973 ◽  
Vol 31 ◽  
pp. 380-381
Author(s):  
S.R. Allegra
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Ultrastructural Study ◽  
The Other ◽  
Blue Nevus ◽  
Normal Complement ◽  
Golgi Vesicles ◽  
Golgi System ◽  
The Subject ◽  
Cellular Blue Nevus

The respective roles of the ribo somes, endoplasmic reticulum, Golgi apparatus and perhaps nucleus in the synthesis and maturation of melanosomes is still the subject of some controversy. While the early melanosomes (premelanosomes) have been frequently demonstrated to originate as Golgi vesicles, it is undeniable that these structures can be formed in cells in which Golgi system is not found. This report was prompted by the findings in an essentially amelanotic human cellular blue nevus (melanocytoma) of two distinct lines of melanocytes one of which was devoid of any trace of Golgi apparatus while the other had normal complement of this organelle.

Acetylcholinesterase in Human Erythroid Cells

1973 ◽  
Vol 12 (3) ◽  
pp. 911-923
Author(s):  
R. J. SKAER
Keyword(s):  
Endoplasmic Reticulum ◽  
Nervous System ◽  
Golgi Apparatus ◽  
Red Cells ◽  
The Other ◽  
Red Cell ◽  
Erythroid Cells ◽  
Cell Replacement ◽  
Kinetics Of ◽  
Human Red Cells

Acetylcholinesterase is present in human red cells but cannot be demonstrated by the copper thiocholine test. The enzyme is revealed, however, in the perinuclear cisterna, endoplasmic reticulum and Golgi apparatus of red cell precursors. It is suggested that 2 forms of the enzyme are present, one of which can be demonstrated by the copper thiocholine test, the other cannot; one form may be the precursor of the other. These observations may cast light on the kinetics of red cell replacement and on the interpretation of the results from the copper thiocholine test on other tissues such as the nervous system.

scholarly journals Capacity of the Golgi Apparatus for Biogenesis from the Endoplasmic Reticulum

2003 ◽  
Vol 14 (12) ◽  
pp. 5011-5018 ◽  
Author(s):  
Sapna Puri ◽  
Adam D. Linstedt
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Self Assembly ◽  
De Novo ◽  
Brefeldin A ◽  
The Other ◽  
Matrix Proteins ◽  
Er Export ◽  
Golgi Matrix

It is unclear whether the mammalian Golgi apparatus can form de novo from the ER or whether it requires a preassembled Golgi matrix. As a test, we assayed Golgi reassembly after forced redistribution of Golgi matrix proteins into the ER. Two conditions were used. In one, ER redistribution was achieved using a combination of brefeldin A (BFA) to cause Golgi collapse and H89 to block ER export. Unlike brefeldin A alone, which leaves matrix proteins in relatively large remnant structures outside the ER, the addition of H89 to BFA-treated cells caused ER accumulation of all Golgi markers tested. In the other, clofibrate treatment induced ER redistribution of matrix and nonmatrix proteins. Significantly, Golgi reassembly after either treatment was robust, implying that the Golgi has the capacity to form de novo from the ER. Furthermore, matrix proteins reemerged from the ER with faster ER exit rates. This, together with the sensitivity of BFA remnants to ER export blockade, suggests that presence of matrix proteins in BFA remnants is due to cycling via the ER and preferential ER export rather than their stable assembly in a matrix outside the ER. In summary, the Golgi apparatus appears capable of efficient self-assembly.

scholarly journals REVERSIBLE ALTERATIONS IN THE GOLGI COMPLEX OF CULTURED NEURONS TREATED WITH AN INHIBITOR OF ACTIVE NA AND K TRANSPORT

1969 ◽  
Vol 42 (2) ◽  
pp. 490-500 ◽  
Author(s):  
William O. Whetsell ◽  
Richard P. Bunge
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Golgi Complex ◽  
Cultured Neurons ◽  
Sensory Ganglia ◽  
Golgi Membrane ◽  
Cytoplasmic Vacuoles ◽  
Golgi System ◽  
A Site ◽  
K Transport

Highly differentiated cultures of rat and mouse sensory ganglia were treated for varying periods (up to 6 hr) with selected doses (1 x 10-3 M to 5 x 10-5 M) of the cardiac glycoside, ouabain (Strophanthin G). This inhibitor of active Na and K transport produced a selective and progressive swelling of elements of the Golgi complex in many, but not all, neurons. After 6 hr of treatment, virtually all Golgi complexes in affected neurons were either altered or absent; large cytoplasmic vacuoles limited by agranular membrane were prominent in these neurons. This response was not observed in satellite cells and Schwann cells. Within a few hours of ouabain withdrawal, the neuronal vacuoles disappeared and normal Golgi areas were again observed. These observations suggest that there is a site for active transport of Na and K on the Golgi membrane of these neurons. In discussing the possible significance of this observation, it is suggested that if this site were directed so that cation was actively pumped from Golgi cisternae into cytoplasm (and if there were differential water and ion permeabilities in various parts of the endoplasmic reticulum-Golgi system), then such a pumping mechanism could provide an explanation for the concentrating function of the Golgi apparatus.

scholarly journals NEURONAL PERIKARYA WITH DISPERSED, SINGLE RIBOSOMES IN THE VISUAL CORTEX OF MACACA MULATTA

1974 ◽  
Vol 63 (3) ◽  
pp. 1074-1089 ◽  
Author(s):  
S. L. Palay ◽  
S. Billings-Gagliardi ◽  
V. Chan-Palay
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Synthesis ◽  
Visual Cortex ◽  
Golgi Apparatus ◽  
Metabolic Activity ◽  
Macaca Mulatta ◽  
The Other ◽  
Cytoplasmic Matrix ◽  
Unusual Pattern ◽  
Intermediate Cells

Numerous small and medium-sized neuronal perikarya in layers III and IV of the visual cortex display an unusual pattern of ribosomal distribution. Instead of being aggregated in clusters, spirals, rows, and other regular polysomal configurations, the ribosomes, whether free or attached to the endoplasmic reticulum, are randomly dispersed, with no discernible pattern. The endoplasmic reticulum in such cells is reduced to a few (perhaps only one) meandering, broad cisternae, which delimit broad fields of cytoplasmic matrix occupied almost solely by scattered, single ribosomes. The Golgi apparatus is elaborate. Mitochondria are either small and numerous or large and infrequent. The other organelles, including the nucleus and nucleolus, are not remarkable. Axonal terminals synapse in the normal fashion on the surfaces of these cells and their dendrites. Associated with these cells are more numerous intermediate cells in which a few to many polysomal clusters can be found. It is proposed that the neurons with dispersed, single ribosomes are inactive in protein synthesis and that the suspension of such an important metabolic activity is probably temporary. Thus, these cells are considered to be part of a population undergoing cyclic fluctuations in the intensity of protein synthesis that should be correlated with their specific neural behavior.

Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells

1999 ◽  
Vol 112 (19) ◽  
pp. 3399-3412 ◽  
Author(s):  
E. Chanat ◽  
P. Martin ◽  
M. Ollivier-Bousquet
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Mammary Epithelial Cells ◽  
Whey Proteins ◽  
Mammary Epithelial ◽  
The Other ◽  
Soluble Form ◽  
Beta Casein

In lactating mammary epithelial cells, interaction between caseins is believed to occur after their transport out of the endoplasmic reticulum. We show here that, in alpha(S1)-casein-deficient goats, the rate of transport of the other caseins to the Golgi apparatus is highly reduced whereas secretion of whey proteins is not significantly affected. This leads to accumulation of immature caseins in distended rough endoplasmic reticulum cisternae. Casein micelles, nevertheless, were still observed in secretory vesicles. In contrast, no accumulation was found in mammary epithelial cells which lack beta-casein. In mammary epithelial cells secreting an intermediate amount of alpha(S1)-casein, less casein accumulated in the rough endoplasmic reticulum, and the transport of alpha(S1)-casein to the Golgi occurred with kinetics similar to that of control cells. In prolactin-treated mouse mammary epithelial HC11 cells, which do not express alpha(S)-caseins, endoplasmic reticulum accumulation of beta-casein was also observed. The amount of several endoplasmic reticulum-resident proteins increased in conjunction with casein accumulation. Finally, the permeabilization of rough endoplasmic reticulum vesicles allowed the recovery of the accumulated caseins in soluble form. We conclude that optimal export of the caseins out of the endoplasmic reticulum is dependent upon alpha(S1)-casein. Our data suggest that alpha(S1)-casein interacts with the other caseins in the rough endoplasmic reticulum and that the formation of this complex is required for their efficient export to the Golgi.

Cellular Blue Nevus. An Ultrastructural Study

1980 ◽  
Vol 7 (2) ◽  
pp. 109-122 ◽  
Author(s):  
JAG BHAWAN ◽  
WALLACE H. CHANG ◽  
LEE M. EDELSTEIN
Keyword(s):  
Ultrastructural Study ◽  
Blue Nevus ◽  
Cellular Blue Nevus

scholarly journals THE IN VITRO DIFFERENTIATION OF MONONUCLEAR PHAGOCYTES

1966 ◽  
Vol 123 (4) ◽  
pp. 757-766 ◽  
Author(s):  
Zanvil A. Cohn ◽  
Martha E. Fedorko ◽  
James G. Hirsch
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Colloidal Gold ◽  
Hydrolytic Enzymes ◽  
Mononuclear Phagocytes ◽  
Electron Microscopic ◽  
Cytochemical Study ◽  
Electron Microscopic Autoradiography ◽  
Dense Granules ◽  
Golgi Vesicles

A combined morphological, autoradiographic, and cytochemical study at the electron microscope level has been directed towards the formation of electron-opaque granules of cultured macrophages. Labeling of the membrane-bound vesicular structures of pinocytic origin was accomplished with colloidal gold. The initial uptake of gold occurred within micropinocytic vesicles. These electron-lucent vesicles subsequently fused with and discharged their contents into larger pinocytic vacuoles. Colloidal gold was homogeneously distributed in the large pinosomes. In contrast, gold was initially deposited in the periphery of preformed dense granules indicating that these structures were also in constant interaction with the external environment. Colloidal gold was not observed within the cisternae of the endoplasmic reticulum nor within the saccules or vesicles of the Golgi apparatus. There were, however, many small, gold-free vesicles, indistinguishable from Golgi vesicles, which were preferentially aligned about and appeared to fuse with the large pinosomes. The intracellular flow of leucine-H3-labeled protein was followed by electron microscopic autoradiography. After a 15 min pulse of labeled amino acid there was initial labeling of the rough endoplasmic reticulum. Subsequently, much of the label appeared in the Golgi complex. At still later time periods the cytoplasmic dense granules contained the majority of the isotope. Acid phosphatase activity was localized to the dense granules and in the majority of cells to the Golgi apparatus. It is suggested that hydrolytic enzymes are initially synthesized in the endoplasmic reticulum and are then transferred to the Golgi apparatus. Here they are packaged into small Golgi vesicles which represent the primary lysosome of macrophages. The Golgi vesicles subsequently fuse with pinosomes, thereby discharging their hydrolases and forming digestive granules or secondary lysosomes.

scholarly journals Rapid, Endoplasmic Reticulum-independent Diffusion of the Mitotic Golgi Haze

2004 ◽  
Vol 15 (4) ◽  
pp. 1843-1852 ◽  
Author(s):  
Magnus A. B. Axelsson ◽  
Graham Warren
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Fluorescence Microscopy ◽  
Cell Line ◽  
Lateral Diffusion ◽  
Brefeldin A ◽  
Pharmacological Analysis ◽  
Golgi Vesicles ◽  
Video Fluorescence Microscopy ◽  
Golgi Compartment

Early in mitosis, the mammalian Golgi apparatus disassembles, and fluorescence microscopy reveals Golgi clusters and an extensive, nonresolvable haze that either represents scattered vesicles or a merged endoplasmic reticulum (ER)-Golgi compartment. To help decide between these alternatives, we have carried out a combined microscopic and pharmacological analysis, by using a BS-C-1 cell line stably coexpressing ER and Golgi markers. Video fluorescence microscopy showed that these two organelles were morphologically distinguishable at all stages of mitosis, and photobleaching experiments showed that diffusion of the Golgi marker was unaffected by the presence of the ER. Fragmentation of the ER by using filipin III completely blocked diffusion of the ER marker but had no effect on the Golgi marker, unless it was first relocated to the ER by using brefeldin A. The Golgi haze was also studied using BODIPY ceramide. Its diffusion was slower in mitotic Golgi than in mitotic ER, but similar to that of a Golgi enzyme marker in the mitotic Golgi haze or in Golgi vesicles generated by ilimaquinone. Together, these results support the idea that the Golgi and the ER remain separate during mitosis and strongly suggest that Golgi markers move by vesicle diffusion, as opposed to lateral diffusion in continuous membranes.

scholarly journals [Ciliogenesis in the mucous cells of the quail oviduct. I. Ultrastructural study in the laying quail]

1976 ◽  
Vol 71 (2) ◽  
pp. 449-459 ◽  
Author(s):  
D Sandoz ◽  
E Biosvieux-Ulrich
Keyword(s):  
Golgi Apparatus ◽  
Ultrastructural Study ◽  
The Other ◽  
Basal Bodies ◽  
Luminal Epithelium ◽  
Mucous Cells ◽  
Ciliated Cells ◽  
Laying Quail ◽  
Golgi Zone

The luminal epithelium of the oviduct (magnum) of laying quails is composed of ciliated cells and mucous cells. Ciliogenesis was observed in some of the mucous cells. Both centrioles of the diplosome migrate to the top of the cell, and one of them induces the formation of a rudimentary cilium. In some of the other cells, that are filled with mucous granules, the formation of basal bodies by an acentriolar pathway was observed. In these cells, numerous, dense fibrous masses are associated with the forming face of the Golgi apparatus. In the Golgi zone, generative complexes composed of a deuterosome and some forming procentrioles were found. Cilia develop from completed basal bodies. During ciliogenesis, the Golgi apparatus is disorganized, and generally the production of mucous granules is arrested. The nucleus is also modified: it becomes larger and the chromatin is dispersed. It is assumed that mucous cells are able to be transformed into ciliated cells in the oviduct of laying quails.

scholarly journals Homologous Proteins of the Manganese Transporter PAM71 Are Localized in the Golgi Apparatus and Endoplasmic Reticulum

Plants ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 239 ◽  
Author(s):  
Natalie Hoecker ◽  
Anna Honke ◽  
Katharina Frey ◽  
Dario Leister ◽  
Anja Schneider
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Growth Conditions ◽  
The Other ◽  
Chloroplast Envelope ◽  
Wild Type ◽  
Homologous Proteins ◽  
Stunted Growth ◽  
Growth Defects ◽  
Precise Expression

Chloroplast manganese transporter 1 (CMT1) and photosynthesis-affected mutant 71 (PAM71) are two membrane proteins that function sequentially to mediate the passage of manganese across the chloroplast envelope and the thylakoid membrane. CMT1 and PAM71 belong to a small five-member protein family in Arabidopsis thaliana. The other three, photosynthesis-affected mutant 71 like 3 (PML3), PML4 and PML5 are not predicted to reside in chloroplast membranes. In this study, the subcellular localization of PML3:GFP, PML4:GFP and PML5:GFP was determined using transient and stable expression assays. PML3:GFP localizes to the Golgi apparatus, whereas PML4:GFP and PML5:GFP are found in the endoplasmic reticulum. We also examined patterns of PML3, PML4 and PML5 promoter activity. Although the precise expression pattern of each promoter was unique, all three genes were expressed in the leaf vasculature and in roots. Greenhouse grown single mutants pml3, pml4, pml5 and the pml4/pml5 double mutant did not exhibit growth defects, however an inspection of the root growth revealed a difference between pml3 and the other genotypes, including wild-type, in 500 µM manganese growth conditions. Strikingly, overexpression of PML3 resulted in a stunted growth phenotype. Putative functions of PML3, PML4 and PML5 are discussed in light of what is known about PAM71 and CMT1.

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